Platelet Membrane Receptor Proteolysis: Implications for Platelet Function

J.Y. Wu, J.W.M. Heemskerk*, C.C.F.M.J. Baaten

*Corresponding author for this work

Research output: Contribution to journal(Systematic) Review article peer-review

10 Citations (Web of Science)

Abstract

The activities of adhesion and signaling receptors in platelets are controlled by several mechanisms. An important way of regulation is provided by proteolytic cleavage of several of these receptors, leading to either a gain or a loss of platelet function. The proteases involved are of different origins and types: (i) present as precursor in plasma, (ii) secreted into the plasma by activated platelets or other blood cells, or (iii) intracellularly activated and cleaving cytosolic receptor domains. We provide a comprehensive overview of the proteases acting on the platelet membrane. We describe how these are activated, which are their target proteins, and how their proteolytic activity modulates platelet functions. The review focuses on coagulation-related proteases, plasmin, matrix metalloproteinases, ADAM(TS) isoforms, cathepsins, caspases, and calpains. We also describe how the proteolytic activities are determined by different platelet populations in a thrombus and conversely how proteolysis contributes to the formation of such populations.
Original languageEnglish
Article number608391
Number of pages13
JournalFrontiers in cardiovascular medicine
Volume7
DOIs
Publication statusPublished - 8 Jan 2021

Keywords

  • adam
  • calpain
  • calpain cleavage
  • caspase
  • coagulation factors
  • factor-va
  • glycoprotein ib-ix
  • hemostatic function
  • in-vitro
  • integrin alpha(iib)beta(3)
  • matrix metalloproteinases
  • mmp
  • platelets
  • procoagulant activity
  • protease-activated receptor-1
  • receptor proteolysis
  • thrombin
  • INTEGRIN ALPHA(IIB)BETA(3)
  • HEMOSTATIC FUNCTION
  • ADAM
  • IN-VITRO
  • FACTOR-VA
  • CALPAIN CLEAVAGE
  • PROTEASE-ACTIVATED RECEPTOR-1
  • PROCOAGULANT ACTIVITY
  • THROMBIN
  • GLYCOPROTEIN IB-IX
  • MMP
  • MATRIX METALLOPROTEINASES

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